[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; DOI=10.1016/S1357-2725(00)00073-X; PubMed=11240369 [NCBI, ExPASy, EBI, Israel, Japan] Lizano S., Lambeau G., Lazdunski M.; "Cloning and cDNA sequence analysis of Lys(49) and Asp(49) basic phospholipase A(2) myotoxin isoforms from Bothrops asper."; Int. J. Biochem. Cell Biol. 33:127-132(2001).
[2]	PROTEIN SEQUENCE OF 17-138, FUNCTION, AND SUBUNIT. TISSUE=Venom; DOI=10.1016/0003-9861(90)90266-2; PubMed=2327788 [NCBI, ExPASy, EBI, Israel, Japan] Kaiser I.I., Gutierrez J.M., Plummer D., Aird S.D., Odell G.V.; "The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops asper."; Arch. Biochem. Biophys. 278:319-325(1990).
[3]	FUNCTION. DOI=10.1016/0041-0101(84)90144-2; PubMed=6426093 [NCBI, ExPASy, EBI, Israel, Japan] Gutierrez J.M., Ownby C.L., Odell G.V.; "Isolation of a myotoxin from Bothrops asper venom: partial characterization and action on skeletal muscle."; Toxicon 22:115-128(1984).
[4]	LETHAL DOSE. PubMed=2873948 [NCBI, ExPASy, EBI, Israel, Japan] Gutierrez J.M., Lomonte B., Chaves F., Moreno E., Cerdas L.; "Pharmacological activities of a toxic phospholipase A isolated from the venom of the snake Bothrops asper."; Comp. Biochem. Physiol. 84C:159-164(1986).
[5]	FUNCTION. DOI=10.1016/0167-4889(93)90080-9; PubMed=8218369 [NCBI, ExPASy, EBI, Israel, Japan] Butron E., Ghelestam M., Gutierrez J.M.; "Effects on cultured mammalian cells of myotoxin III, a phospholipase A2 isolated from Bothrops asper (terciopelo) venom."; Biochim. Biophys. Acta 1179:253-259(1993).
[6]	FUNCTION. DOI=10.1016/0041-0101(93)90289-U; PubMed=8456450 [NCBI, ExPASy, EBI, Israel, Japan] Bultron E., Gutierrez J.M., Thelestam M.; "Effects of Bothrops asper (terciopelo) myotoxin III, a basic phospholipase A2, on liposomes and mouse gastrocnemius muscle."; Toxicon 31:217-222(1993).
[7]	FUNCTION. DOI=10.1016/S0041-0101(98)00107-X; PubMed=9839670 [NCBI, ExPASy, EBI, Israel, Japan] Chaves F., Leon G., Alvarado V.H., Gutierrez J.M.; "Pharmacological modulation of edema induced by Lys-49 and Asp-49 myotoxic phospholipases A2 isolated from the venom of the snake Bothrops asper (terciopelo)."; Toxicon 36:1861-1869(1998).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Displays local myotoxic activity and induces a dose-dependent edema. Myotoxic activity is probably related to a molecular region different from the catalytic site, although enzymatic activity greatly enhances myotoxin action.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
TOXIC DOSE: LD₅₀ is 5.6 mg/kg (95ug/16-18g) by intravenous injection and 25 µg/kg (0.42ug/16-18g) by intracerebroventricular injection into mice.
SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases
PIR	S09314; S09314.
3D structure databases
HSSP	P59071; 1OYF. [HSSP ENTRY / PDB]
SMR	P20474; 1-116.
ModBase	P20474.
Family and domain databases
InterPro	IPR016090; Phospholipase_A2. IPR013090; Phospholipase_A2_AS. IPR001211; Phospholipase_A2_euk. Graphical view of domain structure.
Gene3D	G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER	PTHR11716; Phospholipase_A2; 1.
Pfam	PF00068; Phospholip_A2_1; 1. Pfam graphical view of domain structure.
PRINTS	PR00389; PHPHLIPASEA2.
ProDom	PD000303; PhospholipaseA2; 1. [Domain structure / List of seq. sharing at least 1 domain]
SMART	SM00085; PA2c; 1. SMART graphical view of domain structure.
PROSITE	PS00119; PA2_ASP; 1. PS00118; PA2_HIS; 1.
BLOCKS	P20474.
Phylogenomic databases
HOVERGEN	P20474; -.
Other
ProtoNet	P20474.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Myotoxin; Secreted; Signal; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`
`CHAIN`	`17 138`	`122`	`Phospholipase A2.`	`PRO_0000161617`
`ACT_SITE`	`63 63`		`By similarity.`
`ACT_SITE`	`105 105`		`By similarity.`
`METAL`	`43 43`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`45 45`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`46 46`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`64 64`		`Calcium (By similarity).`
`DISULFID`	`42 131`		`By similarity.`
`DISULFID`	`44 60`		`By similarity.`
`DISULFID`	`59 111`		`By similarity.`
`DISULFID`	`65 138`		`By similarity.`
`DISULFID`	`66 104`		`By similarity.`
`DISULFID`	`73 97`		`By similarity.`
`DISULFID`	`91 102`		`By similarity.`

Sequence information

Length: 138 AA [This is the length of the unprocessed precursor]

Molecular weight: 15751 Da [This is the MW of the unprocessed precursor]

CRC64: 822EAD31537AC536 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRTLWIMAVL LVGVEGSLIE FAKMILEETK RLPFPYYTTY GCYCGWGGQG QPKDATDRCC 

        70         80         90        100        110        120 
FVHDCCYGKL SNCKPKTDRY SYSRKSGVII CGEGTPCEKQ ICECDKAAAV CFRENLRTYK 

       130 
KRYMAYPDLL CKKPAEKC

P20474 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools